메뉴 건너뛰기




Volumn 8, Issue , 2007, Pages

The subunit composition of human extracellular superoxide dismutase (EC-SOD) regulate enzymatic activity

Author keywords

[No Author keywords available]

Indexed keywords

HETERODIMER; HOMODIMER; SUPEROXIDE DISMUTASE; TETRAMER; ANTIOXIDANT; PROTEIN SUBUNIT; SOD3 PROTEIN, HUMAN; UNCLASSIFIED DRUG;

EID: 36649020276     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-8-19     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 0026476480 scopus 로고
    • Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells
    • 1332049
    • Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells. JD Crapo T Oury C Rabouille JW Slot LY Chang, Proc Natl Acad Sci U S A 1992 89 10405 10409 1332049
    • (1992) Proc Natl Acad Sci U S a , vol.89 , pp. 10405-10409
    • Crapo, J.D.1    Oury, T.2    Rabouille, C.3    Slot, J.W.4    Chang, L.Y.5
  • 2
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • 11507097
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. A Okado-Matsumoto I Fridovich, J Biol Chem 2001 276 38388 38393 11507097
    • (2001) J Biol Chem , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 3
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. a physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • 11500508
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. LA Sturtz K Diekert LT Jensen R Lill VC Culotta, J Biol Chem 2001 276 38084 38089 11500508
    • (2001) J Biol Chem , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 4
    • 0021745377 scopus 로고
    • Extracellular superoxide dismutase in human tissues and human cell lines
    • 6541229
    • Extracellular superoxide dismutase in human tissues and human cell lines. SL Marklund, J Clin Invest 1984 74 1398 1403 6541229
    • (1984) J Clin Invest , vol.74 , pp. 1398-1403
    • Marklund, S.L.1
  • 5
    • 0021218456 scopus 로고
    • Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species
    • 6487268
    • Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species. SL Marklund, Biochem J 1984 222 649 655 6487268
    • (1984) Biochem J , vol.222 , pp. 649-655
    • Marklund, S.L.1
  • 6
    • 0028245094 scopus 로고
    • Immunocytochemical localization of extracellular superoxide dismutase in human lung
    • 8015293
    • Immunocytochemical localization of extracellular superoxide dismutase in human lung. TD Oury LY Chang SL Marklund BJ Day JD Crapo, Lab Invest 1994 70 889 898 8015293
    • (1994) Lab Invest , vol.70 , pp. 889-898
    • Oury, T.D.1    Chang, L.Y.2    Marklund, S.L.3    Day, B.J.4    Crapo, J.D.5
  • 7
    • 0030007683 scopus 로고    scopus 로고
    • Extracellular superoxide dismutase in vessels and airways of humans and baboons
    • 8743981
    • Extracellular superoxide dismutase in vessels and airways of humans and baboons. TD Oury BJ Day JD Crapo, Free Radic Biol Med 1996 20 957 965 8743981
    • (1996) Free Radic Biol Med , vol.20 , pp. 957-965
    • Oury, T.D.1    Day, B.J.2    Crapo, J.D.3
  • 8
    • 0020374498 scopus 로고
    • Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase
    • 7175933
    • Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase. JA Tainer ED Getzoff KM Beem JS Richardson DC Richardson, J Mol Biol 1982 160 181 217 7175933
    • (1982) J Mol Biol , vol.160 , pp. 181-217
    • Tainer, J.A.1    Getzoff, E.D.2    Beem, K.M.3    Richardson, J.S.4    Richardson, D.C.5
  • 9
    • 0023026982 scopus 로고
    • Crystallographic characterization of recombinant human CuZn superoxide dismutase
    • 3782115
    • Crystallographic characterization of recombinant human CuZn superoxide dismutase. HE Parge ED Getzoff CS Scandella RA Hallewell JA Tainer, J Biol Chem 1986 261 16215 16218 3782115
    • (1986) J Biol Chem , vol.261 , pp. 16215-16218
    • Parge, H.E.1    Getzoff, E.D.2    Scandella, C.S.3    Hallewell, R.A.4    Tainer, J.A.5
  • 10
    • 0006157248 scopus 로고
    • Human copper-containing superoxide dismutase of high molecular weight
    • 6961438
    • Human copper-containing superoxide dismutase of high molecular weight. SL Marklund, Proc Natl Acad Sci U S A 1982 79 7634 7638 6961438
    • (1982) Proc Natl Acad Sci U S a , vol.79 , pp. 7634-7638
    • Marklund, S.L.1
  • 11
    • 1842709537 scopus 로고
    • Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase
    • 3476950
    • Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. K Hjalmarsson SL Marklund A Engstrom T Edlund, Proc Natl Acad Sci U S A 1987 84 6340 6344 3476950
    • (1987) Proc Natl Acad Sci U S a , vol.84 , pp. 6340-6344
    • Hjalmarsson, K.1    Marklund, S.L.2    Engstrom, A.3    Edlund, T.4
  • 12
    • 0030722746 scopus 로고    scopus 로고
    • Subunit interaction in extracellular superoxide dismutase: Effects of mutations in the N-terminal domain
    • 9385637
    • Subunit interaction in extracellular superoxide dismutase: effects of mutations in the N-terminal domain. P Stenlund D Andersson LA Tibell, Protein Sci 1997 6 2350 2358 9385637
    • (1997) Protein Sci , vol.6 , pp. 2350-2358
    • Stenlund, P.1    Andersson, D.2    Tibell, L.A.3
  • 13
    • 2542509037 scopus 로고    scopus 로고
    • Determination of the structural role of the N-terminal domain of human extracellular superoxide dismutase by use of protein fusions
    • 8547348
    • Determination of the structural role of the N-terminal domain of human extracellular superoxide dismutase by use of protein fusions. LA Tibell E Skarfstad BH Jonsson, Biochim Biophys Acta 1996 1292 47 52 8547348
    • (1996) Biochim Biophys Acta , vol.1292 , pp. 47-52
    • Tibell, L.A.1    Skarfstad, E.2    Jonsson, B.H.3
  • 15
    • 0029992837 scopus 로고    scopus 로고
    • The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid
    • 8643556
    • The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid. LM Carlsson SL Marklund T Edlund, Proc Natl Acad Sci U S A 1996 93 5219 5222 8643556
    • (1996) Proc Natl Acad Sci U S a , vol.93 , pp. 5219-5222
    • Carlsson, L.M.1    Marklund, S.L.2    Edlund, T.3
  • 16
    • 0026730835 scopus 로고
    • The heparin binding site of human extracellular-superoxide dismutase
    • 1637178
    • The heparin binding site of human extracellular-superoxide dismutase. T Adachi T Kodera H Ohta K Hayashi K Hirano, Arch Biochem Biophys 1992 297 155 161 1637178
    • (1992) Arch Biochem Biophys , vol.297 , pp. 155-161
    • Adachi, T.1    Kodera, T.2    Ohta, H.3    Hayashi, K.4    Hirano, K.5
  • 17
    • 0026667737 scopus 로고
    • The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity
    • 1517248
    • The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity. J Sandstrom L Carlsson SL Marklund T Edlund, J Biol Chem 1992 267 18205 18209 1517248
    • (1992) J Biol Chem , vol.267 , pp. 18205-18209
    • Sandstrom, J.1    Carlsson, L.2    Marklund, S.L.3    Edlund, T.4
  • 20
    • 0033591243 scopus 로고    scopus 로고
    • The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis
    • 10329680
    • The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis. JJ Enghild IB Thogersen TD Oury Z Valnickova P Hojrup JD Crapo, J Biol Chem 1999 274 14818 14822 10329680
    • (1999) J Biol Chem , vol.274 , pp. 14818-14822
    • Enghild, J.J.1    Thogersen, I.B.2    Oury, T.D.3    Valnickova, Z.4    Hojrup, P.5    Crapo, J.D.6
  • 24
    • 8344274382 scopus 로고    scopus 로고
    • The structure of rabbit extracellular superoxide dismutase differs from the human protein.
    • 15518578
    • The structure of rabbit extracellular superoxide dismutase differs from the human protein. SV Petersen AV Due Z Valnickova TD Oury JD Crapo JJ Enghild, Biochemistry 2004 43 14275 14281 15518578
    • (2004) Biochemistry , vol.43 , pp. 14275-14281
    • Petersen, S.V.1    Due, A.V.2    Valnickova, Z.3    Oury, T.D.4    Crapo, J.D.5    Enghild, J.J.6
  • 25
    • 0024411652 scopus 로고
    • Evolution of CuZn superoxide dismutase and the Greek key beta-barrel structural motif
    • 2798409
    • Evolution of CuZn superoxide dismutase and the Greek key beta-barrel structural motif. ED Getzoff JA Tainer MM Stempien GI Bell RA Hallewell, Proteins 1989 5 322 336 2798409
    • (1989) Proteins , vol.5 , pp. 322-336
    • Getzoff, E.D.1    Tainer, J.A.2    Stempien, M.M.3    Bell, G.I.4    Hallewell, R.A.5
  • 26
    • 33745161382 scopus 로고    scopus 로고
    • Allosteric Disulfide Bonds
    • 16768438
    • Allosteric Disulfide Bonds. B Schmidt L Ho PJ Hogg, Biochemistry 2006 45 7429 7433 16768438
    • (2006) Biochemistry , vol.45 , pp. 7429-7433
    • Schmidt, B.1    Ho, L.2    Hogg, P.J.3
  • 27
    • 0025775214 scopus 로고
    • Glycosylation of extracellular superoxide dismutase studied by high- performance liquid chromatography and mass spectrometry
    • 1939427
    • Glycosylation of extracellular superoxide dismutase studied by high- performance liquid chromatography and mass spectrometry. M Stromqvist J Holgersson B Samuelsson, J Chromatogr 1991 548 293 301 1939427
    • (1991) J Chromatogr , vol.548 , pp. 293-301
    • Stromqvist, M.1    Holgersson, J.2    Samuelsson, B.3
  • 28
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • 2407068
    • Molecular and cellular aspects of thiol-disulfide exchange. HF Gilbert, Adv Enzymol Relat Areas Mol Biol 1990 63 69 172 2407068
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 29
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • 11524675
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. AL Lamb AS Torres TV O'Halloran AC Rosenzweig, Nat Struct Biol 2001 8 751 755 11524675
    • (2001) Nat Struct Biol , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 30
    • 1842782787 scopus 로고    scopus 로고
    • Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase
    • 15064408
    • Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase. NM Brown AS Torres PE Doan TV O'Halloran, Proc Natl Acad Sci U S A 2004 101 5518 5523 15064408
    • (2004) Proc Natl Acad Sci U S a , vol.101 , pp. 5518-5523
    • Brown, N.M.1    Torres, A.S.2    Doan, P.E.3    O'Halloran, T.V.4
  • 31
    • 0030014041 scopus 로고    scopus 로고
    • Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: A simplified, high-yield purification of extracellular superoxide dismutase
    • 8694786
    • Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase. TD Oury JD Crapo Z Valnickova JJ Enghild, Biochem J 1996 317 51 57 8694786
    • (1996) Biochem J , vol.317 , pp. 51-57
    • Oury, T.D.1    Crapo, J.D.2    Valnickova, Z.3    Enghild, J.J.4
  • 32
    • 0019792891 scopus 로고
    • Analysis of protein and peptide mixtures. Evaluation of three sodium dodecyl sulfate-polyacrylamide gel electrophoresis buffer systems
    • Analysis of protein and peptide mixtures. Evaluation of three sodium dodecyl sulfate-polyacrylamide gel electrophoresis buffer systems. AF Bury, J Chromatogr 1981 213 491 500
    • (1981) J Chromatogr , vol.213 , pp. 491-500
    • Bury, A.F.1
  • 33
    • 36649001044 scopus 로고    scopus 로고
    • GPMAW Home. http://www.gpmaw.com
    • GPMAW Home


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.